ID F6G7T2_RALS8 Unreviewed; 361 AA.
AC F6G7T2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN Name=ttuC2 {ECO:0000313|EMBL:AEG71211.1};
GN OrderedLocusNames=RSPO_m00572 {ECO:0000313|EMBL:AEG71211.1};
OS Ralstonia solanacearum (strain Po82).
OG Plasmid {ECO:0000313|Proteomes:UP000007953}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1031711 {ECO:0000313|EMBL:AEG71211.1, ECO:0000313|Proteomes:UP000007953};
RN [1] {ECO:0000313|EMBL:AEG71211.1, ECO:0000313|Proteomes:UP000007953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Po82 {ECO:0000313|Proteomes:UP000007953};
RX PubMed=21685279; DOI=10.1128/JB.05384-11;
RA Xu J., Zheng H.J., Liu L., Pan Z.C., Prior P., Tang B., Xu J.S., Zhang H.,
RA Tian Q., Zhang L.Q., Feng J.;
RT "Complete genome sequence of the plant pathogen Ralstonia solanacearum
RT strain Po82.";
RL J. Bacteriol. 193:4261-4262(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:18365, ChEBI:CHEBI:15361, ChEBI:CHEBI:15588,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.83;
CC Evidence={ECO:0000256|ARBA:ARBA00001361};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; CP002820; AEG71211.1; -; Genomic_DNA.
DR RefSeq; WP_014618848.1; NC_017575.1.
DR AlphaFoldDB; F6G7T2; -.
DR KEGG; rsn:RSPO_m00572; -.
DR PATRIC; fig|1031711.3.peg.3797; -.
DR HOGENOM; CLU_031953_0_1_4; -.
DR Proteomes; UP000007953; Plasmid megaplasmid.
DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011829; TTC_DH.
DR NCBIfam; TIGR02089; TTC; 1.
DR PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Plasmid {ECO:0000313|EMBL:AEG71211.1}.
FT DOMAIN 5..349
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 361 AA; 39276 MW; A90431C3FE4899C7 CRC64;
MKTYRIATIP GDGIGKEVVP AGRTVMEALA ATGAGLRFAF ENFEWGGDYY RQHGVMMPED
GLDALRDKDA ILFGSAGDAR IPDHITLWGL RLKICQGFDQ YANVRPTRIL PGIDAPLKRC
RAEDLDWVIV RENSEGEYAG VGGRVHQGHP IEAATDVSMM TRAGVERIMR FAFRLAQSRP
RKLLTVITKS NAQRHAMVMW DEIAVQISRE FPDVTWDKEL VDAATARMVN RPASLDTIVA
TNLHADILSD LAAALAGSLG IAPTGNVDPE RRYPSMFEPI HGSAFDIMGK GLANPIGTFW
SVVMLLEHLG EQAAARRVML AIEAVTANPA LHTRDLGGQA TTAQVTQAVC DHLAAKQAQA
A
//
